Purification and characterization of the alternative nitrogenase from the photosynthetic bacterium Rhodospirillum rubrum

Journal of Bacteriology

Volumn 178, Issue 5, 1996, Pages 1445-1450

  Davis, Rick ^a   Lehman, Lori ^a,b   Petrovich, Robert ^a,c   Shah, Vinod K ^a   Roberts, Gary P ^a   Ludden, Paul W ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b Biosource Genetics Corp   (United States)

^c FOX CHASE CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NITROGENASE;

ARTICLE; AZOTOBACTER VINELANDII; ENZYME ACTIVATION; ENZYME ANALYSIS; ENZYME PURIFICATION; ENZYME SUBUNIT; GENE CLUSTER; GENETIC CODE; NONHUMAN; PHOTOSYNTHESIS; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT; RHODOSPIRILLUM RUBRUM;

AZOTOBACTER VINELANDII; BACTERIA (MICROORGANISMS); PHOTOBACTERIA; RHODOSPIRILLUM RUBRUM;

EID: 0029914814     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.178.5.1445-1450.1996     Document Type: Article

References (39)

1. Allen, R. M., M. J. Homer, R. Chatterjee, P. W. Ludden, G. P. Roberts, and V. K. Shah. 1993. Dinitrogenase reductase- and MgATP-dependent maturation of apodinitrogenase from Azotobacter vinelandu J Biol. Chem. 268: 23670-23674.
2. Bishop, P. E. Personal communication.
3. Bishop, P. E., D. M. L. Jarlenski, and D. R. Hetherington. 1980. Evidence for an alternative nitrogen fixation system in Azotobacter vinelandu. Proc. Nat. Acad. Sci. USA 77:7342-7346.
4. Bishop, P. E., and R. D. Joerger. 1990. Genetics and molecular biology of alternative nitrogen fixation systems. Annu. Rev. Plant Physiol. Plant Mol. Biol. 41:109-125.
5. Bishop, P. E., and R. Premakumar. 1992. Alternative nitrogen fixation systems, p. 736-762. In G. Stacey, R. H Burris, and H. J. Evans (ed.), Biological nitrogen fixation. Chapman & Hall, New York.
6. Burns, R. H. 1972. Nitrogen fixation - assay methods and techniques, p. 415-431. In A. San Pietro (ed.), Photosynthesis and nitrogen fixation. Academic Press, New York.
7. Chisnell, J. R., R. Premakumar, and P. E. Bishop. 1988. Purification of a second alternative nitrogenase from a mfHDK deletion strain of Azotobacter vinelandii. J. Bacteriol. 170:27-33.
8. Dean, D. R., J. T. Bolin, and L. Zheng. 1993. Nitrogenase metalloclusters: structures, organization, and synthesis. J. Bacteriol. 175:6737-6744.
9. Dilworth, M. J., R. R. Eady, and M. E. Eldridge. 1988. The vanadium nitrogenase of Azotobacter chroococcum: reduction of acetylene and ethylene to ethane. Biochem. J. 249:745-751.
10. Dilworth, M. J., R. R. Eady, R. L. Robson, and R. W. Miller. 1987. Ethane formation from acetylene as a potential test for vanadium nitrogenase in vivo. Nature (London) 327:167-168.
11. Eady, R. R. 1991. New nitrogenases, p. 255-284. In R. W. Hay, J. R. Dillworth, and K. B. Nolan (ed.), Perspectives on bioinorganic chemistry. JAI Press, Ltd., Greenwich, Conn.
12. Eady, R. R., T. H. Richardson, R. W. Miller, M. Hawkins, and D. J. Lowe. 1988. The vanadium nitrogenase of Azotobacter chroococcum. Biochem. J. 256:189-196.
13. Gollan, U., K. Schneider, A. Müller, K. Schüddekopf, and W. Klipp. 1993. Detection of the in vivo incorporation of a metal cluster into a protein - the FeMo cofactor is inserted into the FeFe protein of the alternative nitrogenase of Rhodobacter capsulants. Eur. J. Biochem. 215:25-35.
14. Hales, B. J., A. E. True, and B. M. Hoffman. 1989 Detection of a new signal in the EPR spectrum of vanadium nitrogenase from Azotobacter vinelandii. J. Am. Chem. Soc. 111:8519-8520.
15. Hoover, T. R., A. D. Robertson, R. L. Cerny, R. N. Hayes, J. Imperial, V. K. Shah, and P. W. Ludden. 1987. Identification of the V factor needed for synthesis of the iron-molybdenum cofactor of nitrogenase as homocitrate. Nature (London) 329:855-857.
16. Joerger, R. D., and P. E. Bishop. 1988. Nucleotide sequence and genetic analysis of the mfB-mfQ region from Azotobacter vinelandii. J. Bacteriol. 170:1475-1487.
17. Joerger, R. D., M. R. Jacobson, R. Premakumar, E. D. Wolfinger, and P. E. Bishop. 1989. Nucleotide sequence and mutational analysis of the structural genes (anfHDGK) for the second alternative nitrogenase from Azotobacter vinelandii. J. Bacteriol. 171:1075-1086.
18. Joerger, R. D., T. M. Loveless, R. N. Pau, L. A. Mitchenall, B. H. Simon, and P. E. Bishop. 1990. Nucleotide sequences and mutational analysis of the structural genes for nitrogenase 2 of Azotobacter vinelandii. J. Bacteriol. 172:3400-3408.
19. Kanemoto, R. H., and P. W. Ludden. 1984. Effect of ammonia, darkness, and phenazine methosulfate on whole-cell nitrogenase activity and Fe protein modification in Rhodospirillum rubrum. J Bacteriol. 158:713-720.
20. Kennedy, C., and D. Dean. 1992. The mfU, nifS and mfV gene products are required for activity of all three nitrogenases of Azotobacter vinelandii. Mol. Gen. Genet. 231:494-498.
21. Kentemich, T., G. Danneberg, B. Hundeshagen, and H. Bothe. 1988. Evidence for the occurrence of the alternative, vanadium-containing nitrogenase in the cyanobacterium Anabaena variabilis. FEMS Microbiol. Lett. 51:19-24
22. Lehman, L. J., and G. P. Roberts. 1991. Identification of an alternative nitrogenase system in Rhodospirillum rubrum. J. Bacteriol. 173:5705-5711.
23. Ludden, P. W., and R. H. Burris. 1976. Activating factor for the iron protein of nitrogenase from Rhodospirillum rubrum. Science 194:424-426.
24. Ludden, P. W., and R. H. Burris. 1978. Purification and properties of nitrogenase from Rhodospirillum rubrum. Evidence for the presence of phosphate, ribose and an adenine-like unit covalently bound to the Fe protein. Biochem. J. 175:251-259.
25. Ma, L., N. Gavini, H. I. Liu, B. Hedman, K. O. Hodgson, and B. K. Burgess. 1994. Large scale isolation and characterization of the molybdenum-iron cluster from nitrogenase. J. Biol. Chem 269:18007-18015.
26. Morningstar, J. E., and B. J. Hales. 1987. Electron paramagnetic resonance study of the vanadium-iron protein of nitrogenase from Azotobacter vinelandii. J. Am. Chem. Soc. 109:6854-6855.
27. Paschinger, H. 1974. A changed nitrogenase activity in Rhodospirillum rubrun after substitution of tungsten for molybdenum. Arch. Microbiol. 101:379-389.
28. Pierik, A. J., D. J. Lowe, M. E. Eldridge, Marritt, S., J. A. Farrar, A. J. Thomson, and R. R. Eady. 1992 EPR and MCD spectroscopic characterisation of the VFe-cofactor and P-cluster centres of the VFe protein from Azotobacter chroococcum, p. 305. In R. Palacios, J. Mora, and W. E. Newton (ed.), New horizons in nitrogen fixation. Proceedings of the 9th International Congress on Nitrogen Fixation. Kiuwer Academic Publishers, Dordrecht, The Netherlands.
29. Premakumar, R., J. R. Chisnell, and P. E. Bishop. 1989. A comparison of the three dinitrogenase reductases expressed by Azotobacter vinelandii. Can. J. Microbiol. 35:344-348.
30. Robson, R. L., R. R. Eady, T. H. Richardson, R. W. Miller, M. Hawkins, and J. R. Postgate. 1986. The alternative nitrogenase of Azotobacter chroococcum is a vanadium enzyme. Nature (London) 322:388-390
31. Robson, R. L., P. R. Woodley, R. N. Pau, and R. R. Eady. 1989. Structural genes for the vanadium nitrogenase from Azotobacter chroococcum EMBO J. 8:1217-1224.
32. Rodríguez-Quiñones, F., R. Bosch, and J. Imperial. 1993. Expression of the nifBfdxNnifOQ region of Azotobacter vinelandii and its role in nitrogenase activity. J. Baeteriol. 175:2926-2935.
33. Schneider, K., A. Muller, U. Schramm, and W. Klipp. 1991. Demonstration of a molybdenum- and vanadium-independent nitrogenase in a nifHDK-deletion mutant of Rhodobacter capsulatus. Eur. J. Biochem. 195:653-661.
34. Scott, D. J., H. D. May, W. E. Newton, K. E. Brigle, and D. R. Dean. 1990. Role for the nitrogenase MoFe protein α-subunit in FeMo-cofactor binding and catalysis. Nature (London) 343:188-190.
35. Shah, V. K., and W. J. Brill. 1977. Isolation of an iron-molybdenum cofactor from nitrogenase. Proc. Natl. Acad. Sci. USA 74:3249-3253.
36. Shah, V. K., J. Imperial, R. A. Ugalde, P. W. Ludden, and W. J. Brill. 1985. In vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Proc. Natl. Acad. Sci. USA 83:1636-1640.
37. Smith, B. E., R. R. Eady, D. J. Lowe, and C. Gormal. 1988. The vanadium-iron protein of vanadium nitrogenase from Azotobacter chroococcum contains an iron-vanadium cofactor. Biochem. J. 250:299-302.
38. 2 fixation using the acetylene reduction technique. Proc. Natl Acad. Sci. USA 58:2071-2078.
39. Walker, G. A., and L. E. Mortenson. 1973. An effect of magnesium adenosine 5′-triphosphate on the structure of azoferredoxin from Clostridium pasteurianum. Biochem. Biophys. Res. Commun. 53:904-909.